A0JUS3 (DXR_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-deoxy-D-xylulose 5-phosphate reductoisomerase
Short name=DXP reductoisomerase
EC=1.1.1.267

Alternative name(s):
1-deoxyxylulose-5-phosphate reductoisomerase
2-C-methyl-D-erythritol 4-phosphate synthase

Gene names

Name:	dxr
Ordered Locus Names:	Arth_1399

Organism

Arthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]

Taxonomic identifier

290399 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP) By similarity. HAMAP MF_00183
Catalytic activity	2-C-methyl-D-erythritol 4-phosphate + NADP+ = 1-deoxy-D-xylulose 5-phosphate + NADPH. HAMAP MF_00183
Cofactor	Divalent cation By similarity. HAMAP MF_00183
Pathway	Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6. HAMAP MF_00183
Sequence similarities	Belongs to the DXR family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis
Ligand	Metal-binding NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-deoxy-D-xylulose-5-phosphate reductoisomerase activity Inferred from electronic annotation. Source: EC NADPH binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	1-deoxy-D-xylulose 5-phosphate reductoisomerase HAMAP MF_00183		PRO_1000020215
Regions
	Nucleotide binding	9 – 38	30	NADP By similarity
Sites
	Metal binding	156	1	Divalent metal cation By similarity
	Metal binding	158	1	Divalent metal cation By similarity
	Metal binding	227	1	Divalent metal cation By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	182	1	Substrate By similarity
	Binding site	205	1	Substrate By similarity
	Binding site	227	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0JUS3 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 392C63832C6F55DE	FASTA	394	41,156
	10 20 30 40 50 60 MQPRRIVLLG STGSIGTQAI DVVDGAPHLF EVVALSAGGG NLELLARQAV HTKAKAVGTA 70 80 90 100 110 120 SGDATALQRL IDDAARATGV AGYRPEIITG PDASTRIAEI EADVVLNGIT GSIGLAPTLA 130 140 150 160 170 180 ALKSGATLAL ANKESLIVGG ALVKAAAREG QIVPVDSEHS AIAQCLRSGT AAEVDRLILT 190 200 210 220 230 240 ASGGPFRGRT REELHNVSPE EALAHPTWDM GLMVTTNSAS LVNKGLEVIE AHLLFDIPLD 250 260 270 280 290 300 RIDVVVHPQS VVHSMVQFVD GSIIAQASPP DMRLPIALGL GWPDRVPKAA TPCDWTQATS 310 320 330 340 350 360 WTFEPLDAEA FPAVNLAKDA AKQGSTYPAV FNAANEEAVM AFHAGRIRFT DIVDTIEAVL 370 380 390 SEHPGSSGLT VESVLDAEAW ARARTHERLA VSSL

References

[1]

"Complete sequence of chromosome 1 of Arthrobacter sp. FB24." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FB24.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000454 Genomic DNA. Translation: ABK02793.1.
RefSeq	YP_830893.1. NC_008541.1.
3D structure databases
ProteinModelPortal	A0JUS3.
SMR	A0JUS3. Positions 2-390.
ModBase	Search...
Protein-protein interaction databases
STRING	A0JUS3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4446070.
GenomeReviews	Gene locus Arth_1399 in contig CP000454_GR.
KEGG	art:Arth_1399.
PATRIC	20998089. VBIArtSp72239_1754.
TIGR	Arth_1399.
Phylogenomic databases
eggNOG	COG0743.
HOGENOM	HBG430762.
OMA	IHSMVEY.
PhylomeDB	A0JUS3.
ProtClustDB	PRK05447.
Enzyme and pathway databases
BioCyc	ASP1667:ARTH_1399-MONOMER.
Family and domain databases
HAMAP	MF_00183. DXP_reductoisom. [Tree]
InterPro	IPR003821. DXP_reductoisomerase. IPR013644. DXP_reductoisomerase_C. IPR013512. DXP_reductoisomerase_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00099.
Pfam	PF08436. DXP_redisom_C. 1 hit. PF02670. DXP_reductoisom. 1 hit. [Graphical view]
PIRSF	PIRSF006205. Dxp_reductismrs. 1 hit.
TIGRFAMs	TIGR00243. Dxr. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DXR_ARTS2

Accession

Primary (citable) accession number: A0JUS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 12, 2006
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program